5e22
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5e22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e22 OCA], [http://pdbe.org/5e22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e22 RCSB], [http://www.ebi.ac.uk/pdbsum/5e22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e22 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5e22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e22 OCA], [http://pdbe.org/5e22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e22 RCSB], [http://www.ebi.ac.uk/pdbsum/5e22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e22 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The internal mechanics of proteins-the coordinated motions of amino acids and the pattern of forces constraining these motions-connects protein structure to function. Here we describe a new method combining the application of strong electric field pulses to protein crystals with time-resolved X-ray crystallography to observe conformational changes in spatial and temporal detail. Using a human PDZ domain (LNX2PDZ2) as a model system, we show that protein crystals tolerate electric field pulses strong enough to drive concerted motions on the sub-microsecond timescale. The induced motions are subtle, involve diverse physical mechanisms, and occur throughout the protein structure. The global pattern of electric-field-induced motions is consistent with both local and allosteric conformational changes naturally induced by ligand binding, including at conserved functional sites in the PDZ domain family. This work lays the foundation for comprehensive experimental study of the mechanical basis of protein function. | ||
| + | |||
| + | Electric-field-stimulated protein mechanics.,Hekstra DR, White KI, Socolich MA, Henning RW, Srajer V, Ranganathan R Nature. 2016 Dec 15;540(7633):400-405. doi: 10.1038/nature20571. Epub 2016 Dec 7. PMID:27926732<ref>PMID:27926732</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5e22" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:24, 18 January 2017
The second PDZ domain of Ligand of Numb protein X 2 in the presence of an electric field of ~1 MV/cm along the crystallographic x axis, with eightfold extrapolation of structure factor differences.
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